8csw
From Proteopedia
(Difference between revisions)
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==Local refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complex== | ==Local refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complex== | ||
| - | <StructureSection load='8csw' size='340' side='right'caption='[[8csw]]' scene=''> | + | <StructureSection load='8csw' size='340' side='right'caption='[[8csw]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8csw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSW FirstGlance]. <br> |
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8csw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csw OCA], [https://pdbe.org/8csw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csw RCSB], [https://www.ebi.ac.uk/pdbsum/8csw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csw ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8csw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csw OCA], [https://pdbe.org/8csw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csw RCSB], [https://www.ebi.ac.uk/pdbsum/8csw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Hereditary spherocytosis. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Probably plays an important role in the regulation of erythrocyte shape and mechanical properties. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering. | ||
| + | |||
| + | Architecture of the human erythrocyte ankyrin-1 complex.,Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865<ref>PMID:35835865</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8csw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cali T]] | + | [[Category: Cali, T]] |
| - | [[Category: Clarke | + | [[Category: Clarke, O B]] |
| - | [[Category: Johnston | + | [[Category: Johnston, J D]] |
| - | [[Category: Kim K]] | + | [[Category: Kim, K]] |
| - | [[Category: Noble | + | [[Category: Noble, A J]] |
| - | [[Category: Vallese F]] | + | [[Category: Vallese, F]] |
| - | [[Category: Yen | + | [[Category: Yen, L Y]] |
| + | [[Category: Anion exchange]] | ||
| + | [[Category: Erythrocyte]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Transport protein-structural protein complex]] | ||
Revision as of 18:21, 27 July 2022
Local refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complex
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